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Protein

snRNA-activating protein complex subunit 4

Gene

SNAPC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi317 – 34125H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi424 – 44724H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi476 – 49924H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc

GO - Biological processi

  • gene expression Source: Reactome
  • snRNA transcription Source: ProtInc
  • snRNA transcription from RNA polymerase III promoter Source: UniProtKB
  • snRNA transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription from RNA polymerase III promoter Source: Reactome
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
snRNA-activating protein complex subunit 4
Short name:
SNAPc subunit 4
Alternative name(s):
Proximal sequence element-binding transcription factor subunit alpha
Short name:
PSE-binding factor subunit alpha
Short name:
PTF subunit alpha
snRNA-activating protein complex 190 kDa subunit
Short name:
SNAPc 190 kDa subunit
Gene namesi
Name:SNAPC4Imported
Synonyms:SNAP190Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11137. SNAPC4.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • snRNA-activating protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941Q → A: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. 1 Publication
Mutagenesisi94 – 941Q → L: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. 1 Publication
Mutagenesisi115 – 1151Q → L: Abolishes SNAPC5 binding in the absence of SNAPC1. Minimal effect on SNAPC5 binding in the presence of SNAPC1. 1 Publication
Mutagenesisi1314 – 13141L → A: Abolishes SNAPC2-binding. 1 Publication
Mutagenesisi1355 – 13551L → A: Abolishes SNAPC2-binding. 1 Publication
Mutagenesisi1362 – 13621L → A: Abolishes SNAPC2-binding. 1 Publication
Mutagenesisi1364 – 13641L → A: Abolishes SNAPC2-binding. 1 Publication
Mutagenesisi1369 – 13691L → A: Decreased binding to SNAPC2. 1 Publication

Organism-specific databases

PharmGKBiPA35985.

Polymorphism and mutation databases

BioMutaiSNAPC4.
DMDMi74762223.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14691469snRNA-activating protein complex subunit 4PRO_0000197120Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei68 – 681PhosphoserineCombined sources
Modified residuei1157 – 11571PhosphothreonineCombined sources
Modified residuei1398 – 13981PhosphoserineCombined sources
Modified residuei1400 – 14001PhosphoserineCombined sources
Modified residuei1440 – 14401PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5SXM2.
MaxQBiQ5SXM2.
PaxDbiQ5SXM2.
PRIDEiQ5SXM2.

PTM databases

iPTMnetiQ5SXM2.
PhosphoSiteiQ5SXM2.

Expressioni

Gene expression databases

BgeeiQ5SXM2.
CleanExiHS_SNAPC4.
ExpressionAtlasiQ5SXM2. baseline and differential.
GenevisibleiQ5SXM2. HS.

Organism-specific databases

HPAiHPA046627.

Interactioni

Subunit structurei

Part of the SNAPc complex composed of 5 subunits: SNAPC1, SNAPC2, SNAPC3, SNAPC4 and SNAPC5. SNAPC4 interacts with SNAPC1, SNAPC2, SNAPC5, BRF2 and TBP.3 Publications

Protein-protein interaction databases

BioGridi112505. 12 interactions.
IntActiQ5SXM2. 18 interactions.
MINTiMINT-149201.
STRINGi9606.ENSP00000298532.

Structurei

3D structure databases

ProteinModelPortaliQ5SXM2.
SMRiQ5SXM2. Positions 260-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 28839Myb-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini289 – 34355HTH myb-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini344 – 39552Myb-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini396 – 45156HTH myb-type 2PROSITE-ProRule annotationAdd
BLAST
Domaini452 – 50352HTH myb-type 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni84 – 13350SNAPC5-binding1 PublicationAdd
BLAST
Regioni1281 – 1393113SNAPC2-binding1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi931 – 1264334Pro-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 3 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation
Contains 2 Myb-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0048. Eukaryota.
COG5147. LUCA.
GeneTreeiENSGT00390000001038.
HOGENOMiHOG000231537.
HOVERGENiHBG080315.
InParanoidiQ5SXM2.
KOiK09453.
OMAiQIDTAGC.
OrthoDBiEOG7PVWP2.
PhylomeDBiQ5SXM2.
TreeFamiTF313064.

Family and domain databases

Gene3Di1.10.10.60. 5 hits.
InterProiIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTiSM00717. SANT. 5 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 3 hits.
PROSITEiPS51294. HTH_MYB. 3 hits.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SXM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED
60 70 80 90 100
LDPADPPISE EERWGEASND EDDPKDKTLP EDPETCLQLN MVYQEVIQEK
110 120 130 140 150
LAEANLLLAQ NREQQEELMR DLAGSKGTKV KDGKSLPPST YMGHFMKPYF
160 170 180 190 200
KDKVTGVGPP ANEDTREKAA QGIKAFEELL VTKWKNWEKA LLRKSVVSDR
210 220 230 240 250
LQRLLQPKLL KLEYLHQKQS KVSSELERQA LEKQGREAEK EIQDINQLPE
260 270 280 290 300
EALLGNRLDS HDWEKISNIN FEGSRSAEEI RKFWQNSEHP SINKQEWSRE
310 320 330 340 350
EEERLQAIAA AHGHLEWQKI AEELGTSRSA FQCLQKFQQH NKALKRKEWT
360 370 380 390 400
EEEDRMLTQL VQEMRVGSHI PYRRIVYYME GRDSMQLIYR WTKSLDPGLK
410 420 430 440 450
KGYWAPEEDA KLLQAVAKYG EQDWFKIREE VPGRSDAQCR DRYLRRLHFS
460 470 480 490 500
LKKGRWNLKE EEQLIELIEK YGVGHWAKIA SELPHRSGSQ CLSKWKIMMG
510 520 530 540 550
KKQGLRRRRR RARHSVRWSS TSSSGSSSGS SGGSSSSSSS SSEEDEPEQA
560 570 580 590 600
QAGEGDRALL SPQYMVPDMD LWVPARQSTS QPWRGGAGAW LGGPAASLSP
610 620 630 640 650
PKGSSASQGG SKEASTTAAA PGEETSPVQV PARAHGPVPR SAQASHSADT
660 670 680 690 700
RPAGAEKQAL EGGRRLLTVP VETVLRVLRA NTAARSCTQK EQLRQPPLPT
710 720 730 740 750
SSPGVSSGDS VARSHVQWLR HRATQSGQRR WRHALHRRLL NRRLLLAVTP
760 770 780 790 800
WVGDVVVPCT QASQRPAVVQ TQADGLREQL QQARLASTPV FTLFTQLFHI
810 820 830 840 850
DTAGCLEVVR ERKALPPRLP QAGARDPPVH LLQASSSAQS TPGHLFPNVP
860 870 880 890 900
AQEASKSASH KGSRRLASSR VERTLPQASL LASTGPRPKP KTVSELLQEK
910 920 930 940 950
RLQEARAREA TRGPVVLPSQ LLVSSSVILQ PPLPHTPHGR PAPGPTVLNV
960 970 980 990 1000
PLSGPGAPAA AKPGTSGSWQ EAGTSAKDKR LSTMQALPLA PVFSEAEGTA
1010 1020 1030 1040 1050
PAASQAPALG PGQISVSCPE SGLGQSQAPA ASRKQGLPEA PPFLPAAPSP
1060 1070 1080 1090 1100
TPLPVQPLSL THIGGPHVAT SVPLPVTWVL TAQGLLPVPV PAVVSLPRPA
1110 1120 1130 1140 1150
GTPGPAGLLA TLLPPLTETR AAQGPRAPAL SSSWQPPANM NREPEPSCRT
1160 1170 1180 1190 1200
DTPAPPTHAL SQSPAEADGS VAFVPGEAQV AREIPEPRTS SHADPPEAEP
1210 1220 1230 1240 1250
PWSGRLPAFG GVIPATEPRG TPGSPSGTQE PRGPLGLEKL PLRQPGPEKG
1260 1270 1280 1290 1300
ALDLEKPPLP QPGPEKGALD LGLLSQEGEA ATQQWLGGQR GVRVPLLGSR
1310 1320 1330 1340 1350
LPYQPPALCS LRALSGLLLH KKALEHKATS LVVGGEAERP AGALQASLGL
1360 1370 1380 1390 1400
VRGQLQDNPA YLLLRARFLA AFTLPALLAT LAPQGVRTTL SVPSRVGSES
1410 1420 1430 1440 1450
EDEDLLSELE LADRDGQPGC TTATCPIQGA PDSGKCSASS CLDTSNDPDD
1460
LDVLRTRHAR HTRKRRRLV
Length:1,469
Mass (Da):159,433
Last modified:December 21, 2004 - v1
Checksum:i78CBCFB1887E106C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1046 – 10461A → G in AAC02972 (PubMed:9418884).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441D → N.
Corresponds to variant rs7031489 [ dbSNP | Ensembl ].
VAR_059455
Natural varianti799 – 7991H → Q.
Corresponds to variant rs3812571 [ dbSNP | Ensembl ].
VAR_050193
Natural varianti1448 – 14481P → S.
Corresponds to variant rs3812561 [ dbSNP | Ensembl ].
VAR_050194

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032387 mRNA. Translation: AAC02972.1.
AL592301 Genomic DNA. Translation: CAI13935.1.
CCDSiCCDS6998.1.
PIRiT09219.
RefSeqiNP_003077.2. NM_003086.2.
XP_005266153.1. XM_005266096.1.
XP_006717304.1. XM_006717241.1.
XP_006717305.1. XM_006717242.2.
UniGeneiHs.113265.

Genome annotation databases

EnsembliENST00000298532; ENSP00000298532; ENSG00000165684.
GeneIDi6621.
KEGGihsa:6621.
UCSCiuc004chh.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032387 mRNA. Translation: AAC02972.1.
AL592301 Genomic DNA. Translation: CAI13935.1.
CCDSiCCDS6998.1.
PIRiT09219.
RefSeqiNP_003077.2. NM_003086.2.
XP_005266153.1. XM_005266096.1.
XP_006717304.1. XM_006717241.1.
XP_006717305.1. XM_006717242.2.
UniGeneiHs.113265.

3D structure databases

ProteinModelPortaliQ5SXM2.
SMRiQ5SXM2. Positions 260-499.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112505. 12 interactions.
IntActiQ5SXM2. 18 interactions.
MINTiMINT-149201.
STRINGi9606.ENSP00000298532.

PTM databases

iPTMnetiQ5SXM2.
PhosphoSiteiQ5SXM2.

Polymorphism and mutation databases

BioMutaiSNAPC4.
DMDMi74762223.

Proteomic databases

EPDiQ5SXM2.
MaxQBiQ5SXM2.
PaxDbiQ5SXM2.
PRIDEiQ5SXM2.

Protocols and materials databases

DNASUi6621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000298532; ENSP00000298532; ENSG00000165684.
GeneIDi6621.
KEGGihsa:6621.
UCSCiuc004chh.4. human.

Organism-specific databases

CTDi6621.
GeneCardsiSNAPC4.
H-InvDBHIX0008543.
HIX0201404.
HGNCiHGNC:11137. SNAPC4.
HPAiHPA046627.
MIMi602777. gene.
neXtProtiNX_Q5SXM2.
PharmGKBiPA35985.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0048. Eukaryota.
COG5147. LUCA.
GeneTreeiENSGT00390000001038.
HOGENOMiHOG000231537.
HOVERGENiHBG080315.
InParanoidiQ5SXM2.
KOiK09453.
OMAiQIDTAGC.
OrthoDBiEOG7PVWP2.
PhylomeDBiQ5SXM2.
TreeFamiTF313064.

Enzyme and pathway databases

ReactomeiR-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

ChiTaRSiSNAPC4. human.
GeneWikiiSNAPC4.
GenomeRNAii6621.
NextBioi25787.
PROiQ5SXM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SXM2.
CleanExiHS_SNAPC4.
ExpressionAtlasiQ5SXM2. baseline and differential.
GenevisibleiQ5SXM2. HS.

Family and domain databases

Gene3Di1.10.10.60. 5 hits.
InterProiIPR009057. Homeodomain-like.
IPR017877. Myb-like_dom.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF00249. Myb_DNA-binding. 2 hits.
[Graphical view]
SMARTiSM00717. SANT. 5 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 3 hits.
PROSITEiPS51294. HTH_MYB. 3 hits.
PS50090. MYB_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The large subunit of basal transcription factor SNAPc is a Myb domain protein that interacts with Oct-1."
    Wong M.W., Henry R.W., Ma B., Kobayashi R., Klages N., Matthias P., Strubin M., Hernandez N.
    Mol. Cell. Biol. 18:368-377(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SNAPC2.
    Tissue: TeratocarcinomaImported.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "A map of protein-protein contacts within the small nuclear RNA-activating protein complex SNAPc."
    Ma B., Hernandez N.
    J. Biol. Chem. 276:5027-5035(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAPC1; SNAPC2 AND SNAPC5, MUTAGENESIS OF GLN-94; GLN-115; LEU-1314; LEU-1355; LEU-1362; LEU-1364 AND LEU-1369.
  4. "The small nuclear RNA-activating protein 190 Myb DNA binding domain stimulates TATA box-binding protein-TATA box recognition."
    Hinkley C.S., Hirsch H.A., Gu L., LaMere B., Henry R.W.
    J. Biol. Chem. 278:18649-18657(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TBP AND BRF2.
  5. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1398 AND SER-1400, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSNPC4_HUMAN
AccessioniPrimary (citable) accession number: Q5SXM2
Secondary accession number(s): Q9Y6P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: December 21, 2004
Last modified: April 13, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.